Protein Antimicrobial Barriers to Bacterial Adhesion
Open Access
- 1 October 1998
- journal article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 81 (10) , 2771-2778
- https://doi.org/10.3168/jds.s0022-0302(98)75835-7
Abstract
The ability of microorganisms to adhere to solid surfaces is a problem of high visibility and has been the focus of numerous investigations because these organisms can cause disease and food spoilage. During the last several years, considerable attention has been focused on the development of food-grade antimicrobial barriers to adhesion in order to inhibit the initial adhesion of microbial contaminants by application of an antimicrobial agent to the surface rather than trying to remove these contaminants once they are adhered. The premise is that, if both the presence of the agent and its antimicrobial activity are maintained at the interface, sensitive bacterial cells or spores that attempt to attach would be killed. Nisin has been used in foods as a direct additive to inhibit the growth of Gram-positive cells and spores. Similarly, hen lysozyme is a commercially available antimicrobial protein that offers application in food processing systems, but the mode of action of this enzyme differs from that of nisin. We have shown that nisin can adsorb to surfaces, maintain activity, and kill cells that have adhered. In addition, we have addressed questions relating to the short- and long-term stability of adsorbed nisin, the degree to which immobilized nisin can resist exchange with dissolved solution components, and the surface concentrations that are necessary to inhibit biofilm formation. More recently, we have focused on basic questions relating to molecular influences on antimicrobial activity at interfaces using synthetic mutants of bacteriophage T4 lysozyme and hen lysozyme in addition to nisin.Keywords
This publication has 25 references indexed in Scilit:
- Models of protein adsorption on solid surfacesPublished by Springer Nature ,2007
- Structural Changes of T4 Lysozyme upon Adsorption to Silica Nanoparticles Measured by Circular DichroismJournal of Colloid and Interface Science, 1995
- Relationships between conformational stabilities and surface functional properties of mutant hen egg-white lysozymes constructed by genetic engineeringJournal of Agricultural and Food Chemistry, 1994
- The elutability of fibrinogen by sodium dodecyl sulphate and alkyltrimethylammonium bromidesColloids and Surfaces A: Physicochemical and Engineering Aspects, 1993
- Circular dichroism studies on conformational changes in protein molecules upon adsorption on ultrafine polystyrene particlesBiotechnology & Bioengineering, 1992
- Structure of adsorbed and desorbed proteinsColloids and Surfaces, 1992
- Multilayer adsorption of lysozyme on a hydrophobic substrateBiophysical Journal, 1990
- Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3Nature, 1988
- IS FLEMING'S LYSOZYME AN ANALGESIC AGENT? EXPERIMENTS ON MICEClinical and Experimental Pharmacology and Physiology, 1983
- 446. A note on the inhibition of an anaerobic sporeformer in Swiss-type cheese by a nisin-producing streptococcusJournal of Dairy Research, 1951